Article
Exploring Folding Aspects of Monomeric Superoxide Dismutase.
The journal of physical chemistry. B - 30 Jan 2020
Mouro Paulo R, Povinelli Ana P R, Leite Vitor B P, Chahine Jorge
Abstract excerpt
Recent studies have associated the absence of bound metals (Apo protein) and mutations in Cu-Zn Human Superoxide Dismutase (SOD1) with amyotrophic lateral sclerosis (ALS) disease, suggesting mechanisms of SOD1 aggregation. Using a structure-based model and modifying the energy of interaction between amino acids in the metal-binding site, we detected differences between the folding of the apo and holo proteins....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
